UniProt ID | PD1L2_HUMAN | |
---|---|---|
UniProt AC | Q9BQ51 | |
Protein Name | Programmed cell death 1 ligand 2 | |
Gene Name | PDCD1LG2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 273 | |
Subcellular Localization |
Isoform 3: Secreted . Isoform 2: Endomembrane system Single-pass type I membrane protein . Isoform 1: Cell membrane Single-pass type I membrane protein . |
|
Protein Description | Involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production (By similarity).. | |
Protein Sequence | MIFLLLMLSLELQLHQIAALFTVTVPKELYIIEHGSNVTLECNFDTGSHVNLGAITASLQKVENDTSPHRERATLLEEQLPLGKASFHIPQVQVRDEGQYQCIIIYGVAWDYKYLTLKVKASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQSQMEPRTHPTWLLHIFIPFCIIAFIFIATVIALRKQLCQKLYSSKDTTKRPVTTTKREVNSAI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
9 | Phosphorylation | IFLLLMLSLELQLHQ HHHHHHHHHHHHHHH | 13.06 | 24719451 | |
22 | Phosphorylation | HQIAALFTVTVPKEL HHHHHHHEEEECCEE | 19.00 | 24719451 | |
37 | N-linked_Glycosylation | YIIEHGSNVTLECNF EEEECCCCEEEEEEC | 35.07 | UniProtKB CARBOHYD | |
64 | N-linked_Glycosylation | ASLQKVENDTSPHRE EEEHHHHCCCCCHHH | 61.93 | UniProtKB CARBOHYD | |
114 | Phosphorylation | GVAWDYKYLTLKVKA EEEECCEEEEEEEHE | 9.93 | - | |
116 | Phosphorylation | AWDYKYLTLKVKASY EECCEEEEEEEHEEE | 22.80 | - | |
128 | Phosphorylation | ASYRKINTHILKVPE EEEEECEEEEEECCC | 17.48 | - | |
157 | N-linked_Glycosylation | LAEVSWPNVSVPANT EEEEECCCEECCCCC | 32.22 | UniProtKB CARBOHYD | |
159 | Phosphorylation | EVSWPNVSVPANTSH EEECCCEECCCCCCC | 29.08 | - | |
163 | N-linked_Glycosylation | PNVSVPANTSHSRTP CCEECCCCCCCCCCC | 35.72 | UniProtKB CARBOHYD | |
165 | Phosphorylation | VSVPANTSHSRTPEG EECCCCCCCCCCCCC | 21.19 | - | |
167 | Phosphorylation | VPANTSHSRTPEGLY CCCCCCCCCCCCCEE | 37.30 | - | |
169 | Phosphorylation | ANTSHSRTPEGLYQV CCCCCCCCCCCEEEE | 28.80 | 29978859 | |
174 | Phosphorylation | SRTPEGLYQVTSVLR CCCCCCEEEEEEEEE | 16.28 | 29978859 | |
177 | Phosphorylation | PEGLYQVTSVLRLKP CCCEEEEEEEEEECC | 9.52 | 29978859 | |
178 | Phosphorylation | EGLYQVTSVLRLKPP CCEEEEEEEEEECCC | 21.94 | 29978859 | |
189 | N-linked_Glycosylation | LKPPPGRNFSCVFWN ECCCCCCCEEEEEEC | 38.81 | UniProtKB CARBOHYD |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of PD1L2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PD1L2_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PD1L2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PD1L2_HUMAN !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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